S. L. Reck-Peterson

Development of LRRK2 designed ankyrin-repeat proteins

This study develops a high-affinity DARPin that binds to LRRK2's WD40 domain, improving structural analysis and revealing its role in disrupting LRRK2 filaments and Rab8A phosphorylation.

Woronin bodies move dynamically and bidirectionally by hitchhiking on early endosomes in Aspergillus nidulans

The paper shows Woronin bodies in Aspergillus nidulans move by hitchhiking on early endosomes, and this movement is dependent on PxdA, though not essential for their septal function.

Structure of LRRK1 and mechanisms of autoinhibition and activation

This study solves cryo-EM structures of LRRK1 in monomeric and dimeric forms, revealing distinct autoinhibition mechanisms compared to LRRK2 and their evolutionary context.

Lis1 relieves cytoplasmic dynein-1 auto-inhibition by acting as a molecular wedge

The paper presents a structure showing Lis1 relieves dynein-1 auto-inhibition by acting as a molecular wedge, revealing its role in dynein activation.

Structures of human cytoplasmic dynein in complex with the lissencephaly 1 protein, LIS1

The paper reports cryo-EM structures of human dynein-LIS1 complexes, revealing differences from yeast and mapping disease mutations.

Antiviral function and viral antagonism of the rapidly evolving dynein activating adapter NINL

This study identifies NINL as an antiviral innate immune component targeted by viruses through proteolytic cleavage, revealing its role in interferon response and viral antagonism.

Lis1 binding regulates force-induced detachment of cytoplasmic dynein from microtubules

This study shows Lis1 binding to dynein affects force-induced detachment asymmetry and slows dynein movement without altering stall forces.

Structural basis for Parkinson's Disease-linked LRRK2's binding to microtubules

This study determines the structural basis of LRRK2's microtubule binding, identifies key residues involved, and shows their disruption affects binding without impacting kinase activity.

Cytoplasmic dynein-1 cargo diversity is mediated by the combinatorial assembly of FTS-Hook-FHIP complexes

The paper investigates how dynein cargo diversity is achieved through the combinatorial assembly of FTS-Hook-FHIP complexes in human cells.

Structural Basis for Cytoplasmic Dynein-1 Regulation by Lis1

This study presents the first high-resolution structure of the yeast dynein-Lis1 complex, revealing molecular interactions essential for Lis1's regulation of dynein function across species.

Optimizing microtubule arrangements for rapid cargo capture

The paper models diffusive cargo capture along microtubules in tubular cells, showing that optimal microtubule arrangements with a single long microtubule and broad plus-end distribution minimize capture times.

PxdA interacts with the DipA phosphatase to regulate endosomal hitchhiking of peroxisomes

The paper identifies PxdA as a specific molecular linker for peroxisome hitchhiking on early endosomes in A. nidulans and reveals DipA as a regulator of this process.

Parkinson's Disease-linked LRRK2 structure and model for microtubule interaction

This study reports the structure of LRRK2 and its interaction with microtubules, showing that its conformation regulates binding and affects motor protein function.

Hitching a Ride: Mechanics of Organelle Transport Through Linker-Mediated Hitchhiking

The paper develops a quantitative model to study hitchhiking transport of organelles in fungal hyphae, showing how linker proteins and cytoskeletal tracks affect transport efficiency.

Lis1 promotes the formation of maximally activated cytoplasmic dynein-1 complexes

This paper identifies Lis1's role in forming maximally activated dynein complexes by binding to dynein's motor domain, enhancing microtubule binding and velocity.

HOOK3 is a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein and KIF1C

This study identifies HOOK3 as a scaffold that links cytoplasmic dynein and KIF1C, enabling bidirectional transport by coupling opposite-polarity microtubule-based motors.

Lis1 has two opposing modes of regulating cytoplasmic dynein

This study reveals that Lis1 regulates cytoplasmic dynein through two opposing modes of microtubule-binding affinity, dependent on Lis1 stoichiometry and dynein's nucleotide state.

The Human Cytoplasmic Dynein Interactome Reveals Novel Activators Of Motility

The paper identifies ninein and ninein-like as new dynein activators using BioID, revealing their role in cargo binding and motility.